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UniProtKB - P99024 (TBB5_MOUSE)

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Protein

Tubulin beta-5 chain

Gene

Tubb5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

  • cellular process Source: MGI
  • microtubule-based process Source: MGI
  • protein folding Source: Reactome
  • spindle assembly Source: MGI
Complete GO annotation...

Keywordsi

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-389967. Formation of tubulin folding intermediates by CCT/TriC.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-5 chain
Gene namesi
Name:Tubb5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:107812. Tubb5.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic ribonucleoprotein granule Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • membrane raft Source: Ensembl
  • microtubule Source: MGI
  • microtubule cytoskeleton Source: MGI
  • nuclear envelope lumen Source: MGI
  • nucleus Source: MGI
  • tubulin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Disruption phenotypei

Results in a perturbation of the cell cycle of neurogenic progenitors as well as an alteration in the position of migrating neurons. There is a decrease in neurons in the cortical plate and an accumulation of cells within the ventricular and intermediate zones.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi172S → A: Loss of CDK1-mediated phosphorylation. 1 Publication1
Mutagenesisi172S → D or E: Mimics phosphorylation, unable to incorporate into microtubules. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482461 – 444Tubulin beta-5 chainAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1
Modified residuei55PhosphothreonineBy similarity1
Modified residuei58N6-acetyllysine; alternateCombined sources1
Modified residuei58N6-succinyllysine; alternateCombined sources1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.1 Publication
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:15890843). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity).By similarity1 Publication
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP99024.
MaxQBiP99024.
PaxDbiP99024.
PeptideAtlasiP99024.
PRIDEiP99024.
TopDownProteomicsiP99024.

2D gel databases

REPRODUCTION-2DPAGEiIPI00117352.
P99024.
SWISS-2DPAGEiP99024.

PTM databases

iPTMnetiP99024.
PhosphoSitePlusiP99024.
SwissPalmiP99024.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in spleen, thymus and immature brain. Expressed in embryonic brain, including throughout the developing cortex and in the subventricular zone. Also found in radial glial cells, intermediate progenitors, migrating neurons and postmitotic neurons (PubMed:23246003). Expressed in skin and developing hair follicle (PubMed:26637975).2 Publications

Gene expression databases

BgeeiENSMUSG00000001525.
CleanExiMM_TUBB5.
ExpressionAtlasiP99024. baseline and differential.
GenevisibleiP99024. MM.

Interactioni

Subunit structurei

Heterodimer of alpha and beta chains (By similarity). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO (PubMed:20643351). Interacts with DIAPH1 (By similarity). Interacts with MX1 (By similarity). May interact with RNABP10 (PubMed:18347012). Interacts with CFAP157 (PubMed:27965440).By similarity3 Publications

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

BioGridi204381. 28 interactors.
IntActiP99024. 37 interactors.
MINTiMINT-1869561.
STRINGi10090.ENSMUSP00000001566.

Structurei

3D structure databases

ProteinModelPortaliP99024.
SMRiP99024.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375. Eukaryota.
COG5023. LUCA.
GeneTreeiENSGT00760000119061.
HOVERGENiHBG000089.
InParanoidiP99024.
KOiK07375.
OMAiIARQNCH.
OrthoDBiEOG091G06U2.
PhylomeDBiP99024.
TreeFamiTF300298.

Family and domain databases

Gene3Di3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiView protein in InterPro
IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiView protein in Pfam
PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiView protein in SMART
SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiView protein in PROSITE
PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.

Sequencei

Sequence statusi: Complete.

P99024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY 
        60         70         80         90        100
YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 
       110        120        130        140        150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL 
       160        170        180        190        200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 
       210        220        230        240        250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 
       260        270        280        290        300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 
       310        320        330        340        350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 
       360        370        380        390        400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 
       410        420        430        440 
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Length:444
Mass (Da):49,671
Last modified:August 13, 1987 - v1
Checksum:i1E6CD0A36773A103
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15Q → P in BAB27292 (PubMed:16141072).Curated1
Sequence conflicti114D → N in BAE40217 (PubMed:16141072).Curated1
Sequence conflicti143T → N in BAE28709 (PubMed:16141072).Curated1
Sequence conflicti264H → D in BAE40217 (PubMed:16141072).Curated1
Sequence conflicti307H → N in BAE39835 (PubMed:16141072).Curated1
Sequence conflicti357P → T in BAE40217 (PubMed:16141072).Curated1
Sequence conflicti400G → A in AAA40510 (PubMed:3839797).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04663 mRNA. Translation: CAA28369.1.
AK010960 mRNA. Translation: BAB27292.1.
AK011263 mRNA. Translation: BAB27504.1.
AK051164 mRNA. Translation: BAC34541.1.
AK051393 mRNA. Translation: BAC34623.1.
AK083327 mRNA. Translation: BAC38866.1.
AK146567 mRNA. Translation: BAE27265.1.
AK148978 mRNA. Translation: BAE28709.1.
AK151215 mRNA. Translation: BAE30210.1.
AK151670 mRNA. Translation: BAE30596.1.
AK160225 mRNA. Translation: BAE35700.1.
AK161575 mRNA. Translation: BAE36471.1.
AK165249 mRNA. Translation: BAE38103.1.
AK167691 mRNA. Translation: BAE39738.1.
AK167779 mRNA. Translation: BAE39811.1.
AK167808 mRNA. Translation: BAE39835.1.
AK167926 mRNA. Translation: BAE39931.1.
AK168271 mRNA. Translation: BAE40217.1.
AK169123 mRNA. Translation: BAE40903.1.
AK169210 mRNA. Translation: BAE40982.1.
AK169295 mRNA. Translation: BAE41051.1.
CR974451 Genomic DNA. Translation: CAO77890.1.
BC003825 mRNA. Translation: AAH03825.1.
M28732 mRNA. Translation: AAA40510.1.
CCDSiCCDS28706.1.
PIRiE25437.
RefSeqiNP_035785.1. NM_011655.5.
UniGeneiMm.273538.
Mm.472638.

Genome annotation databases

EnsembliENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
GeneIDi22154.
KEGGimmu:22154.
UCSCiuc008ciq.2. mouse.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiTBB5_MOUSE
AccessioniPrimary (citable) accession number: P99024
Secondary accession number(s): B1B178
, P05218, Q3TFB6, Q3THH9, Q3TIL1, Q3UAV4, Q3UF52, Q8WUC1, Q9CY33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 7, 2017
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families